Stimulus-responsive assembly of nonviral nucleocapsids
Mao Hori,
Angela Steinauer,
Stephan Tetter,
Jamiro Hälg,
Eva-Maria Manz and
Donald Hilvert ()
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Mao Hori: ETH Zürich
Angela Steinauer: ETH Zürich
Stephan Tetter: ETH Zürich
Jamiro Hälg: ETH Zürich
Eva-Maria Manz: ETH Zürich
Donald Hilvert: ETH Zürich
Nature Communications, 2024, vol. 15, issue 1, 1-10
Abstract:
Abstract Controlled assembly of a protein shell around a viral genome is a key step in the life cycle of many viruses. Here we report a strategy for regulating the co-assembly of nonviral proteins and nucleic acids into highly ordered nucleocapsids in vitro. By fusing maltose binding protein to the subunits of NC-4, an engineered protein cage that encapsulates its own encoding mRNA, we successfully blocked spontaneous capsid assembly, allowing isolation of the individual monomers in soluble form. To initiate RNA-templated nucleocapsid formation, the steric block can be simply removed by selective proteolysis. Analyses by transmission and cryo-electron microscopy confirmed that the resulting assemblies are structurally identical to their RNA-containing counterparts produced in vivo. Enzymatically triggered cage formation broadens the range of RNA molecules that can be encapsulated by NC-4, provides unique opportunities to study the co-assembly of capsid and cargo, and could be useful for studying other nonviral and viral assemblies.
Date: 2024
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-47808-1
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DOI: 10.1038/s41467-024-47808-1
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